A Soluble Form of the High Affinity IgE Receptor, Fc-Epsilon-RI, Circulates in Human Serum
2011

Soluble IgE Receptor Found in Human Serum

Sample size: 119 publication 10 minutes Evidence: moderate

Author Information

Author(s): Dehlink Eleonora, Platzer Barbara, Baker Alexandra H., LaRosa Jessica, Pardo Michael, Dwyer Peter, Yen Elizabeth H., Szépfalusi Zsolt, Nurko Samuel, Fiebiger Edda

Primary Institution: Harvard Medical School, Children's Hospital Boston

Hypothesis

Is there a soluble form of the high affinity IgE receptor, FcεRI, in human serum?

Conclusion

The study identifies a soluble form of the FcεRI alpha-chain in human serum that can inhibit IgE binding to cell surface receptors.

Supporting Evidence

  • sFcεRI levels correlate with serum IgE in patients with elevated IgE.
  • sFcεRI can block binding of IgE to FcεRI expressed at the cell surface.
  • sFcεRI is found as both a free form and bound to IgE in human serum.
  • The study established a novel ELISA for detecting sFcεRI.

Takeaway

Scientists found a new type of IgE receptor in the blood that can help control allergies by blocking IgE from attaching to cells.

Methodology

The study used immunoprecipitation and ELISA to detect and quantify soluble FcεRI in serum samples from children with varying IgE levels.

Potential Biases

Potential bias due to the lack of a healthy control group in the patient cohort.

Limitations

The study did not include healthy individuals, limiting the ability to draw broader conclusions about sFcεRI's clinical relevance.

Participant Demographics

119 children (56 boys, 63 girls, mean age 10.6 years) with a range of normal and elevated serum IgE levels.

Statistical Information

P-Value

0.106

Statistical Significance

p<0.05

Digital Object Identifier (DOI)

10.1371/journal.pone.0019098

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